Other names published for RPS23A: S12, S23A, S28A, YS14, rp37, ribosomal 40S subunit protein S23A, YGR118W
RPS23A LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
RPS23A - Protein-protein Interactions (10)
| Reference | Other Genes Addressed |
|---|---|
| Karaskova M, et al. (2012) Functional characterization of the role of the N-terminal domain of the c/Nip1 subunit of eukaryotic initiation factor 3 (eIF3) in AUG recognition. J Biol Chem 287(34):28420-34 | |
| Becker T, et al. (2011) Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome. Nat Struct Mol Biol 18(6):715-20 | |
| Elantak L, et al. (2010) The Indispensable N-Terminal Half of eIF3j/HCR1 Cooperates with its Structurally Conserved Binding Partner eIF3b/PRT1-RRM and with eIF1A in Stringent AUG Selection. J Mol Biol 396(4):1097-1116 | |
| Kuroha K, et al. (2010) Receptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest. EMBO Rep 11(12):956-61 | |
| Nanda JS, et al. (2009) eIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation. J Mol Biol 394(2):268-85 | |
| Passmore LA, et al. (2007) The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. Mol Cell 26(1):41-50 | |
| Fekete CA, et al. (2005) The eIF1A C-terminal domain promotes initiation complex assembly, scanning and AUG selection in vivo. EMBO J 24(20):3588-601 | |
| Spahn CM, et al. (2004) Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation. EMBO J 23(5):1008-19 | |
| George R, et al. (2002) The nascent polypeptide-associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo. FEBS Lett 516(1-3):213-6 | |
| Menetret JF, et al. (2000) The structure of ribosome-channel complexes engaged in protein translocation. Mol Cell 6(5):1219-32 |



